Fractionation profiling: a fast and versatile approach for mapping vesicle proteomes and protein-protein interactions.
Bottom Line: Functionally associated groups of proteins are revealed through cluster analysis.Of importance, the cluster analysis extends to all profiled proteins and thus identifies a diverse range of known and novel cytosolic and membrane-associated protein complexes.In addition, it provides a versatile tool for the rapid generation of large-scale protein interaction maps.
Affiliation: Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany firstname.lastname@example.org.Show MeSH
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Mentions: The foregoing data demonstrate the predictive power of our approach for known protein complexes. However, profiling also predicts the existence of novel complexes (Figure 5, Supplemental Figure S2, and Supplemental Table S5). For example, we provide the first evidence that the BAR-domain proteins SNX4 and SNX30 (van Weering etÂ al., 2010) form a stable dimer (Figure 5, A and B). A recent study identified a novel protein dimer C17orf75/WDR11, implicated in protection against ricin toxicity (Bassik etÂ al., 2013). Our profiling data suggest that these proteins are in fact part of a trimeric complex, which also includes the protein FAM91A1 (Figure 5, C and D). The protein C10orf32 has been implicated in susceptibility to arsenic poisoning (Pierce etÂ al., 2012); here we propose that C10orf32 is in complex with the uncharacterized protein LOIH12CR1 (Figure 5, E and F). These examples illustrate that our approach covers a broad spectrum of important novel protein associations.
Affiliation: Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany email@example.com.